生物活性 | |||
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描述 | Histone deacetylases (HDACs) are a class of zinc-dependent amide hydrolases with important biological functions. They catalyze the deacetylation of numerous substrate proteins, including histones, transcription factors, and signaling proteins, and thus regulate various biological processes. SIS17, a HDAC 11 inhibitor with an IC50 value of 0.83 μM, inhibits the demyristoylation of a known HDAC11 substrate, serine hydroxymethyl transferase 2, without inhibiting other HDACs. Using a myristoyl-SHMT2 peptide as the substrate, SIS17 could still inhibit HDAC11 with IC50 value of 270 nM. SIS17 increased the fatty acylation level of SHMT2 significantly in MCF7 cells down to 12.5 μM, demonstrating that it is cell permeable and can inhibit HDAC11 in living cells[1]. |
实验方案 | |||
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1mg | 5mg | 10mg | |
1 mM 5 mM 10 mM |
2.73mL 0.55mL 0.27mL |
13.64mL 2.73mL 1.36mL |
27.28mL 5.46mL 2.73mL |
参考文献 |
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